Somatostatin-28 is a 28-amino acid peptide with the same biological activities of somatostatin-14 but with a 14-amino acid extension at the N-terminal and is the major form of somatostatin in the GASTROINTESTINAL TRACT.
CAT No: 10-101-289
CAS No:74315-46-1
Synonyms/Alias:somatostatin 1-28;SST-28;Somatostatin 28;SRIF-28;74315-46-1;Somatostatin 28,cyclic;CHEMBL501796;GTPL2020;SOMATOSTATIN-28 (SHEEP);GLXC-26294;AKOS024456430;FS109420;H-Ser-Ala-Asn-Ser-Asn-Pro-Ala-Met-Ala-Pro-Arg-Glu-Arg-Lys-Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys-OH; H-SANSNPAMAPRE RKAGCKNFFWKTFTSC-OH;Ser-Ala-Asn-Ser-Asn-Pro-Ala-Met-Ala-Pro-Arg-Glu-Arg-Lys-Ala-Gly-Cys(1)-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys(1)-OH;
Somatostatin-28 is a naturally occurring peptide hormone comprising 28 amino acids, known for its potent inhibitory effects on endocrine and exocrine secretion. As an extended form of somatostatin, it plays a critical role in regulating hormone release and neurotransmission within the central nervous system and peripheral tissues. Its distinctive structure and biological activity make it a valuable subject in biochemical and physiological research, particularly in studies focused on neuroendocrine signaling, peptide-receptor interactions, and the broader somatostatinergic system. Researchers are drawn to its unique properties for exploring mechanisms of hormone regulation, cellular signaling, and the development of novel analytical assays in peptide science.
Neuroendocrine signaling research: Somatostatin-28 is widely utilized in investigations of neuroendocrine pathways, where it serves as a tool to elucidate the mechanisms underlying hormone secretion and feedback inhibition. By applying this peptide in in vitro or ex vivo models, scientists can dissect its influence on the release of growth hormone, insulin, glucagon, and other regulatory peptides. Such studies advance the understanding of hypothalamic-pituitary axis function, offering insights into the modulation of endocrine homeostasis and the physiological significance of somatostatinergic tone.
Receptor binding and signaling studies: The peptide's affinity for somatostatin receptor subtypes, particularly SSTR1-SSTR5, enables detailed characterization of receptor-ligand interactions. Researchers employ it to map binding specificity, assess receptor activation, and compare the pharmacological profiles of somatostatin isoforms. These applications are critical for deciphering the structural requirements for receptor engagement and for supporting the rational design of receptor-selective analogs or antagonists in basic and translational research.
Peptide functional assays: Somatostatin-28 is frequently incorporated into functional assays to evaluate its inhibitory effects on cellular secretion, proliferation, and neurotransmitter release. Through cell-based and tissue-based experimental systems, investigators can quantify the peptide's modulatory actions, assess downstream signaling cascades, and explore desensitization or internalization of somatostatin receptors. This approach provides a robust platform for delineating the physiological and pharmacological nuances of peptide-mediated inhibition.
Analytical method development: The well-characterized structure and bioactivity of somatostatin-28 make it an ideal standard or reference material in the development of quantitative analytical techniques. It is commonly used in high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassay validation to calibrate detection systems or to benchmark assay sensitivity and specificity. Such applications are essential for ensuring accurate quantification of somatostatin peptides in complex biological samples, supporting both basic research and quality control processes.
Peptide synthesis and analog development: The extended sequence of somatostatin-28 provides a template for synthetic peptide chemistry and analog design. Researchers leverage its structure to generate modified peptides with altered receptor selectivity, enhanced stability, or tailored biological activity. These efforts facilitate the exploration of structure-activity relationships and support the development of novel research tools or experimental probes to interrogate somatostatinergic pathways. By serving as both a model peptide and a synthetic target, it underpins advances in peptide engineering and functional analysis.
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